PDBe 4j02

X-ray diffraction
2Å resolution

Crystal structure of hcv ns5b polymerase in complex with [(1R)-5,8-DICHLORO-1-PROPYL-1,3,4,9-TETRAHYDROPYRANO[3,4-B]INDOL-1-YL]ACETIC ACID

Released:

Function and Biology Details

Reactions catalysed:
ATP + H(2)O = ADP + phosphate. 
NTP + H(2)O = NDP + phosphate. 
Hydrolysis of four peptide bonds in the viral precursor polyprotein, commonly with Asp or Glu in the P6 position, Cys or Thr in P1 and Ser or Ala in P1'. 
Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1). 
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
RNA-directed RNA polymerase Chains: A, B
Molecule details ›
Chains: A, B
Length: 576 amino acids
Theoretical weight: 64.29 KDa
Source organism: Hepatitis C virus isolate HC-J4
Expression system: Escherichia coli
UniProt:
  • Canonical: O92972 (Residues: 2420-2989; Coverage: 19%)
Sequence domains: Viral RNA dependent RNA polymerase

Ligands and Environments

3 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E SUPERBRIGHT
Spacegroup: P212121
Unit cell:
a: 105.76Å b: 108.34Å c: 133.06Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.195 0.195 0.22
Expression system: Escherichia coli